Non-FG mediated transport of the large pre-ribosomal subunit through the nuclear pore complex by the mRNA export factor Gle2
Autor: | Laura Occhipinti, Stefan Kemmler, Anna Maria Menet, Vikram Govind Panse, Martin Altvater, Yiming Chang |
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Rok vydání: | 2013 |
Předmět: |
Saccharomyces cerevisiae Proteins
Protein subunit Mutant Molecular Sequence Data Active Transport Cell Nucleus Biology Ribosome 03 medical and health sciences Genetics Amino Acid Sequence RNA Messenger Nuclear pore Nuclear export signal Molecular Biology 030304 developmental biology 0303 health sciences Messenger RNA Binding Sites 030302 biochemistry & molecular biology Ribosome Subunits Large Eukaryotic Cell biology Nuclear Pore Complex Proteins Biochemistry Cytoplasm Mutation Nuclear Pore Nucleoporin Sequence Alignment |
Zdroj: | Nucleic Acids Research Nucleic Acids Research, 41 (17) |
ISSN: | 1362-4962 0301-5610 |
Popis: | Multiple export receptors passage bound pre-ribosomes through nuclear pore complexes (NPCs) by transiently interacting with the Phe-Gly (FG) meshwork of their transport channels. Here, we reveal how the non-FG interacting yeast mRNA export factor Gly-Leu-FG lethal 2 (Gle2) functions in the export of the large pre-ribosomal subunit (pre-60S). Structure-guided studies uncovered conserved platforms used by Gle2 to export pre-60S: an uncharacterized basic patch required to bind pre-60S, and a second surface that makes non-FG contacts with the nucleoporin Nup116. A basic patch mutant of Gle2 is able to function in mRNA export, but not pre-60S export. Thus, Gle2 provides a distinct interaction platform to transport pre-60S to the cytoplasm. Notably, Gle2’s interaction platforms become crucial for pre-60S export when FG-interacting receptors are either not recruited to pre-60S or are impaired. We propose that large complex cargos rely on non-FG as well as FG-interactions for their efficient translocation through the nuclear pore complex channel. Nucleic Acids Research, 41 (17) ISSN:1362-4962 ISSN:0301-5610 |
Databáze: | OpenAIRE |
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